Skip to main content
Article thumbnail
Location of Repository

Caspase-9 cleavage: do you need it

By Davina Twiddy and Kelvin Cain


This is the authors' final draft of the commentary published as Biochemical Journal, 2007, 405(1), e1-2, and available from which is activated by association with the Apaf-1 apoptosome complex cleaves and activates the downstream effector caspases-3 and -7, thereby executing the caspase-cascade and cell death programme. Although, caspase-9 does not need to be cleaved to be active, apoptotic cell death is always accompanied by autocatalytic cleavage and by further downstream effector caspase-dependent cleavage of caspase-9. In this issue of the Biochemical Journal, Denault and co-workers evaluate the role of caspase-3-dependent cleavage of caspase-9 and conclude that this mechanism mainly serves to enhance apoptosis by alleviating XIAP inhibition of the apical caspase

Publisher: Portland Press
Year: 2007
OAI identifier:

Suggested articles


  1. (2001). A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis.
  2. (2003). A unified model for apical caspase activation. doi
  3. (2006). Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately doi
  4. (1999). Caspase-9 can be activated without proteolytic processing. doi
  5. (2001). Dimer formation drives the activation of the cell death protease caspase 9. doi
  6. (2005). Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation. doi
  7. (2003). Mechanism of XIAP-mediated inhibition of caspase-9. doi
  8. (2001). Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes. doi
  9. (2000). Structural and biochemical basis of apoptotic activation by Smac/DIABLO.

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.